ReviewMolecules (Basel, Switzerland)2026
Chemical Constructions, Mechanism and Biological Interpretation of Nitroreductase-Responsive Systems: From Hypoxia-Associated Imaging to Activatable Therapy.
Review in Molecules (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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6 authors.
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Abstract
Nitroreductase (NTR)-responsive systems convert the enzymatic reduction of nitroaromatic substrates into detectable signals, molecular retention, supramolecular assembly, or therapeutic activation. Their interpretation is nevertheless complicated by the distinct catalytic properties of bacterial NTRs, experimentally introduced or engineered NTR systems, and endogenous mammalian nitro-reducing enzymes. In particular, an NTR-responsive signal in mammalian tissues should not automatically be interpreted as a direct measurement of oxygen concentration or as evidence for the activity of a single endogenous "NTR." This review analyzes NTR-responsive systems through an integrated framework that connects catalytic source, chemical event, signal-transduction mechanism, and biological application. We first distinguish defined bacterial NTRs, engineered or experimentally introduced NTR systems, and endogenous mammalian nitro-reducing activity. We then describe the recognition, linker, and output modules used in molecular design and compare three major reaction architectures: direct reduction, reduction-triggered cleavage, and reduction-triggered retention or assembly. Photoinduced electron transfer (PET), intramolecular charge transfer (ICT), fluorescence resonance energy transfer (FRET), aggregation-induced emission (AIE), chemiluminescence, photoacoustic imaging, and fluorine nuclear magnetic resonance (
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